The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
Open accessAbstract
Alzheimer's disease and Parkinson's disease are associated with the cerebral accumulation of β-amyloid and α-synuclein, respectively. Some patients have clinical and pathological features of both diseases, raising the possibility of overlapping pathogenetic pathways. We generated transgenic (tg) mice with neuronal expression of human β-amyloid peptides, α-synuclein, or both. The functional and morphological alterations in doubly tg mice resembled the Lewy-body variant of Alzheimer's disease. These mice had severe deficits in learning and memory, developed motor deficits before α-synuclein singly tg mice, and showed prominent age-dependent degeneration of cholinergic neurons and presynaptic terminals. They also had more α-synuclein-immunoreactive neuronal inclusions than α-synuclein singly tg mice. Ultrastructurally, some of these inclusions were fibrillar in doubly tg mice, whereas all inclusions were amorphous in α-synuclein singly tg mice. β-Amyloid peptides promoted aggregation of α-synuclein in a cell-free system and intraneuronal accumulation of α-synuclein in cell culture. β-Amyloid peptides may contribute to the development of Lewy-body diseases by promoting the aggregation of α-synuclein and exacerbating α-synuclein-dependent neuronal pathologies. Therefore, treatments that block the production or accumulation of β-amyloid peptides could benefit a broader spectrum of disorders than previously anticipated.
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“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“The hαSyn/hAPP model recapitulated many of the clinical symptoms and pathology of AD-LBV.”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Further evidence of a link between αSyn and Aβ pathology was offered from studies using mice expressing wt human αSyn (hαSyn) and human APP (hAPP) (hαSyn/hAPP).”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
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Citations
Cites
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
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Self-citationA Drosophila model of Parkinson's disease
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Items 601–607 of 607
Al-Naqeeb, T. H., Al‐Hakeim, H. K., Zhang, Y., & Maes, M. H. J. (2026) · medRxiv · doi:10.64898/2026.03.15.26348456
Développement et caractérisation de nouveaux modèles murins de maladie à corps de Lewy
Schueller, E. (2020) · theses.fr (ABES) · doi:10.70675/4a313736z3f42z4d92zb1c1ze3cbd7bbe9f6
Rabichow, B. E., Nixon, L., Tallant, L., Gibson, K. A., Nascari, D. G., Barnett, J. H., Massa, N., & Fryer, J. D. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71639
Na, H. K., Sun, Y., Park, C. W., Lee, J. H., Choi, Y. Y., Vo, Q. P., Chung, S. J., Yoo, H. S., Lyoo, C. H., Sohn, Y. H., et al. (2026) · Movement Disorders · doi:10.1002/mds.70446
Targeting protein aggregate co-pathologies in neurodegeneration: a viable therapeutic strategy?
Buck, S. A., Madhavan, S. S., & Sanders, L. H. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00047-8
Greimel, S. J. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
Metadata
- Authors
- Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., & Mucke, L.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-09-25
- Volume
- 98
- Issue
- 21
- Pages
- 12245-12250
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC59799
- OpenAlex
- W2131710583
- Cited by
- 607
- References
- 56
- Citations by year
- 2026: 8 · 2025: 26 · 2024: 17 · 2023: 23 · 2022: 17 · 2021: 17 · 2020: 39 · 2019: 26 · 2018: 25 · 2017: 23 · 2016: 24 · 2015: 26 · 2014: 44 · 2013: 29 · 2012: 24
- FWCI
- 15.14
- Type
- journal article
- Language
- en
- Update notices
- correction (2025-05-22)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- National Institutes of Health (AG5131, 5r29ag010869-05, AG‐18440, AG11385, AG10869)
- National Institute on Aging (AG-11385, R37AG018440, R37AG011385, R01AG018440, P50AG005131, AG-5131, AG 18440, AG10869, R01AG011385)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, alpha-synuclein, Alzheimer's disease, Parkinson's disease, Lewy body disease, transgenic mice, neuronal inclusions, alpha-synuclein aggregation, cholinergic neuron degeneration, motor impairment, learning and memory impairment, presynaptic terminals
- MeSH terms
- Age Factors, Alzheimer Disease, Animals, Cell Line, Disease Models, Animal, Female, Humans, Learning Disabilities, Male, Memory Disorders, Mice, Transgenic, Nerve Tissue Proteins, Neurons, Parkinson Disease, Gene Expression, Amyloid beta-Peptides, Mice, Synucleins, alpha-Synuclein
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